Structural and functional study of Streptococcus pyogenes Csn2, CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats)-associated protein

CRISPR-Cas system;Streptococcus pyogenes SF370;Csn2;x-ray crystallography;DNA binding;630

농업생명과학대학 농생명공학부 ;

University:서울대학교 대학원

关键词: CRISPR-Cas system;    Streptococcus pyogenes SF370;    Csn2;    x-ray crystallography;    DNA binding;    630;   

Others  :  http://s-space.snu.ac.kr/bitstream/10371/125790/1/000000003257.pdf

美国|英语

来源: Seoul National University Open Repository

【 摘 要 】

The CRISPR-Cas (clustered regularly interspaced short palindromic repeats-CRISPR-associated proteins) system functions as an adaptive immune system that protects prokaryotic cells from invading genomic nucleic acids, such as bacteriophages and conjugative plasmids. Csn2 is a Nmeni subtype-specific Cas protein, recently classified as type Ⅱ–A, required for new spacer acquisition in the adaptation process of this immune system. In this study, the crystal structure of Streptococcus pyogenes Csn2 revealed a ring-like quaternary structure including calcium binding sites. Also, the Csn2 has a non-specific double-stranded (ds-) DNA-binding activity.In summary, the results support the suggestions of Csn2 functioning at the CRISPR adaptation stage.